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Immunochemical characterization of the modulator protein of the ATP,Mg-dependent protein phosphatase
C Vanden Abeele1, J R Vandenheede, W Merlevede
1Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Belgium.
FEBS Letters
|May 9, 1988
Abstract:
Polyclonal antibodies raised against the modulator protein of the ATP,Mg-dependent protein phosphatase completely neutralize all known properties of the purified modulator: inhibition or inactivation of the phosphatase catalytic subunit as well as the kinase FA-mediated activation of the ATP,Mg-dependent phosphatase. They do not cross-react with phosphoinhibitor-1 or the phosphatase catalytic subunit. Direct analysis of boiled or unboiled skeletal muscle extracts by Western blotting reveals a 32 kDa polypeptide corresponding to the modulator protein as the most dominant protein staining band.